Our research focuses on understanding the molecular mechanisms of membrane proteins and protein-DNA complexes using structural biology approaches. We employ a multidisciplinary strategy that integrates biochemistry, electrophysiology, and structural biology. In parallel, we are committed to developing new methods to address key challenges in the field, with the goal of studying biological macromolecules, particularly membrane proteins, in their native cellular environment.
We determined the cryo-EM structure of human NHA1 (SLC9B1), a sodium/proton antiporter essential for sperm motility and male fertility, in an inward-open state. Key residues bridging the core and gate domains during conformational switching were identified and validated by mutagenesis, transport assays, and MD simulations, offering new insights into sperm motility and male fertility.
Read More →We developed a novel vesicle-based method that preserves the native lipid environment of membrane proteins, which can advance structural and functional studies.
Read More →TMEM63C exists primarily as a monomer under physiological conditions. In contrast, TMEM63B is a mix of monomer and dimer in cells, suggesting that oligomerization is a regulatory mechanism for TMEM63 proteins.
Read More →Our group reports the cryo-EM structure of the cyanophage P-SCSP1u, an MPP-C phage, in its native form at near-atomic resolution, which reveals the assembly mechanism of the capsid and molecular interaction of the portal-tail complex.
Read More →Cryo-EM analysis demonstrates that ZCB11 heavy chain predominantly interacts with Omicron spike trimer with receptor-binding domain in an up conformation, blocking ACE2 binding.
Read More →The hMCM-DH with a constricted central channel untwists and stretches the DNA strands such that almost a half turn of the bound duplex DNA is distorted with 1 base pair completely separated, generating an initial open structure at the hexamer junction.
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